[1]
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NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=8226978 [NCBI, ExPASy, EBI, Israel, Japan]
Selbie L.A.,
Schmitz-Peiffer C.,
Sheng Y.,
Biden T.J.;
"Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells.";
J. Biol. Chem. 268:24296-24302(1993).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Teratocarcinoma;
DOI=10.1016/0888-7543(95)80190-W; PubMed=7607695 [NCBI, ExPASy, EBI, Israel, Japan]
Mazzarella R.,
Ciccodicola A.,
Esposito T.,
Arcucci A.,
Migliaccio C.,
Jones C.,
Schlessinger D.,
D'Urso M.,
D'Esposito M.;
"Human protein kinase C iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3.";
Genomics 26:629-631(1995).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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INTERACTION WITH SMG1, AND ENZYME REGULATION.
PubMed=8524286 [NCBI, ExPASy, EBI, Israel, Japan]
Diaz-Meco M.T.,
Municio M.M.,
Sanchez P.,
Lozano J.,
Moscat J.;
"Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo.";
Mol. Cell. Biol. 16:105-114(1996).
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[5]
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INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION.
PubMed=9566925 [NCBI, ExPASy, EBI, Israel, Japan]
Sanchez P.,
De Carcer G.,
Sandoval I.V.,
Moscat J.,
Diaz-Meco M.T.;
"Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62.";
Mol. Cell. Biol. 18:3069-3080(1998).
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[6]
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INTERACTION WITH SQSTM1 AND IKBKB, AND FUNCTION.
DOI=10.1093/emboj/18.11.3044; PubMed=10356400 [NCBI, ExPASy, EBI, Israel, Japan]
Sanz L.,
Sanchez P.,
Lallena M.-J.,
Diaz-Meco M.T.,
Moscat J.;
"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation.";
EMBO J. 18:3044-3053(1999).
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[7]
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INTERACTION WITH PARD6A; PARD6B AND PARD6G, AND SUBUNIT OF A COMPLEX CONTAINING PARD6B AND CDC42/RAC1.
PubMed=11260256 [NCBI, ExPASy, EBI, Israel, Japan]
Noda Y.,
Takeya R.,
Ohno S.,
Naito S.,
Ito T.,
Sumimoto H.;
"Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C.";
Genes Cells 6:107-119(2001).
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[8]
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INTERACTION WITH PARD3 AND PARD6B IN THE TERNARY AKPC/PAR3/PAR6 COMPLEX.
DOI=10.1083/jcb.152.6.1183; PubMed=11257119 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki A.,
Yamanaka T.,
Hirose T.,
Manabe N.,
Mizuno K.,
Shimizu M.,
Akimoto K.,
Izumi Y.,
Ohnishi T.,
Ohno S.;
"Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures.";
J. Cell Biol. 152:1183-1196(2001).
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[9]
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FUNCTION, AND INTERACTION WITH GAPDH.
DOI=10.1074/jbc.M109744200; PubMed=11724794 [NCBI, ExPASy, EBI, Israel, Japan]
Tisdale E.J.;
"Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway.";
J. Biol. Chem. 277:3334-3341(2002).
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[10]
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PHOSPHORYLATION AT TYR-256; TYR-271 AND TYR-325, AND MUTAGENESIS OF TYR-256; TYR-271 AND TYR-325.
DOI=10.1128/MCB.21.24.8414-8427.2001; PubMed=11713277 [NCBI, ExPASy, EBI, Israel, Japan]
Wooten M.W.,
Vandenplas M.L.,
Seibenhener M.L.,
Geetha T.,
Diaz-Meco M.T.;
"Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase C's via a src kinase pathway.";
Mol. Cell. Biol. 21:8414-8427(2001).
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[11]
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INTERACTION WITH KPNB1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-256, AND MUTAGENESIS OF TYR-256.
DOI=10.1002/jcb.10101.abs; PubMed=11891849 [NCBI, ExPASy, EBI, Israel, Japan]
White W.O.,
Seibenhener M.L.,
Wooten M.W.;
"Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C.";
J. Cell. Biochem. 85:42-53(2002).
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[12]
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INTERACTION WITH CENTA1.
DOI=10.1016/S0006-291X(03)01187-2; PubMed=12893243 [NCBI, ExPASy, EBI, Israel, Japan]
Zemlickova E.,
Dubois T.,
Kerai P.,
Clokie S.,
Cronshaw A.D.,
Wakefield R.I.D.,
Johannes F.-J.,
Aitken A.;
"Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C.";
Biochem. Biophys. Res. Commun. 307:459-465(2003).
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[13]
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INTERACTION WITH PARD6B/PAR-6 AND LLGL1.
DOI=10.1016/S0960-9822(03)00244-6; PubMed=12725730 [NCBI, ExPASy, EBI, Israel, Japan]
Yamanaka T.,
Horikoshi Y.,
Sugiyama Y.,
Ishiyama C.,
Suzuki A.,
Hirose T.,
Iwamatsu A.,
Shinohara A.,
Ohno S.;
"Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity.";
Curr. Biol. 13:734-743(2003).
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[14]
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INTERACTION WITH RAB2.
DOI=10.1074/jbc.M309343200; PubMed=14570876 [NCBI, ExPASy, EBI, Israel, Japan]
Tisdale E.J.;
"Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation.";
J. Biol. Chem. 278:52524-52530(2003).
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[15]
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FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M505402200; PubMed=15994303 [NCBI, ExPASy, EBI, Israel, Japan]
Regala R.P.,
Weems C.,
Jamieson L.,
Copland J.A.,
Thompson E.A.,
Fields A.P.;
"Atypical protein kinase Ciota plays a critical role in human lung cancer cell growth and tumorigenicity.";
J. Biol. Chem. 280:31109-31115(2005).
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[16]
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INTERACTION WITH CDK7, AND SUBCELLULAR LOCATION.
DOI=10.1016/j.tice.2004.10.004; PubMed=15695176 [NCBI, ExPASy, EBI, Israel, Japan]
Bicaku E.,
Patel R.,
Acevedo-Duncan M.;
"Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-iota in human glioma cells.";
Tissue Cell 37:53-58(2005).
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[17]
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INTERACTION WITH RAB2 AND GADPH, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M513031200; PubMed=16452474 [NCBI, ExPASy, EBI, Israel, Japan]
Tisdale E.J.,
Artalejo C.R.;
"Src-dependent aprotein kinase C iota/lambda (aPKCiota/lambda) tyrosine phosphorylation is required for aPKCiota/lambda association with Rab2 and glyceraldehyde-3-phosphate dehydrogenase on pre-golgi intermediates.";
J. Biol. Chem. 281:8436-8442(2006).
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[18]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-403, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T.,
Yi W.,
Lu B.,
Park S.K.,
Xu T.,
Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
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[19]
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STRUCTURE BY NMR OF 16-99, INTERACTION WITH SQSTM1 AND MAP2K5, AND MUTAGENESIS OF LYS-20 AND ASP-63.
DOI=10.1074/jbc.M403092200; PubMed=15143057 [NCBI, ExPASy, EBI, Israel, Japan]
Hirano Y.,
Yoshinaga S.,
Ogura K.,
Yokochi M.,
Noda Y.,
Sumimoto H.,
Inagaki F.;
"Solution structure of atypical protein kinase C PB1 domain and its mode of interaction with ZIP/p62 and MEK5.";
J. Biol. Chem. 279:31883-31890(2004).
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[20]
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X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 16-99 IN COMPLEX WITH PARD6A, AND MUTAGENESIS OF ASP-63; GLU-76 AND ARG-82.
DOI=10.1074/jbc.M409823200; PubMed=15590654 [NCBI, ExPASy, EBI, Israel, Japan]
Hirano Y.,
Yoshinaga S.,
Takeya R.,
Suzuki N.N.,
Horiuchi M.,
Kohjima M.,
Sumimoto H.,
Inagaki F.;
"Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains.";
J. Biol. Chem. 280:9653-9661(2005).
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[21]
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X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 224-587, MASS SPECTROMETRY, AND PHOSPHORYLATION AT THR-403 AND THR-555.
DOI=10.1016/j.jmb.2005.07.060; PubMed=16125198 [NCBI, ExPASy, EBI, Israel, Japan]
Messerschmidt A.,
Macieira S.,
Velarde M.,
Baedeker M.,
Benda C.,
Jestel A.,
Brandstetter H.,
Neuefeind T.,
Blaesse M.;
"Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif.";
J. Mol. Biol. 352:918-931(2005).
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[22]
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VARIANTS [LARGE SCALE ANALYSIS] LEU-109 AND CYS-121.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
Greenman C.,
Stephens P.,
Smith R.,
Dalgliesh G.L.,
Hunter C.,
Bignell G.,
Davies H.,
Teague J.,
Butler A.,
Stevens C.,
Edkins S.,
O'Meara S.,
Vastrik I.,
Schmidt E.E.,
Avis T.,
Barthorpe S.,
Bhamra G.,
Buck G.,
Choudhury B., ![]()
Clements J.,
Cole J.,
Dicks E.,
Forbes S.,
Gray K.,
Halliday K.,
Harrison R.,
Hills K.,
Hinton J.,
Jenkinson A.,
Jones D.,
Menzies A.,
Mironenko T.,
Perry J.,
Raine K.,
Richardson D.,
Shepherd R.,
Small A.,
Tofts C.,
Varian J.,
Webb T.,
West S.,
Widaa S.,
Yates A.,
Cahill D.P.,
Louis D.N.,
Goldstraw P.,
Nicholson A.G.,
Brasseur F.,
Looijenga L.,
Weber B.L.,
Chiew Y.-E.,
DeFazio A.,
Greaves M.F.,
Green A.R.,
Campbell P.,
Birney E.,
Easton D.F.,
Chenevix-Trench G.,
Tan M.-H.,
Khoo S.K.,
Teh B.T.,
Yuen S.T.,
Leung S.Y.,
Wooster R.,
Futreal P.A.,
Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
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